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Q4JHE3 (OXLA_OXYSC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismOxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Taxonomic identifier8667 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Oxyuranus ›

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 517499L-amino-acid oxidase
PRO_5000140378

Regions

Nucleotide binding62 – 632FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding106 – 1094FAD By similarity
Nucleotide binding483 – 4886FAD By similarity
Nucleotide binding483 – 4842Substrate By similarity

Sites

Binding site901FAD By similarity
Binding site1091Substrate By similarity
Binding site2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3911Substrate By similarity
Binding site4761FAD By similarity

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 192 By similarity
Disulfide bond350 ↔ 431 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JHE3 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 1509F4998BFD08A2

FASTA51759,070
        10         20         30         40         50         60 
MNVFFMFSLL FLAALESCAD VRRNPLEECF READYEEFLE IARNGLKKTS NPKHVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LAGAGHKVTL LEASERVGGR VHTYRNEKEG WYVNLGPMRL PERHRIIREY 

       130        140        150        160        170        180 
IRKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL 

       190        200        210        220        230        240 
KKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL 

       250        260        270        280        290        300 
KSDDLFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEKV RVAYQTPAKT 

       310        320        330        340        350        360 
LSYVTADYVI VCSSSRAARR IYFEPPLPPK KAHALRSIHY KSGTKIFLTC SKKFWEADGI 

       370        380        390        400        410        420 
HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YTISDDADFF QSLDIKTSAD IVINDLSLIH 

       430        440        450        460        470        480 
QLPKKEIQAL CYPSMIKKWS LDKYAMGSIT SFAPYQFQDF IERVAAPVGR IYFAGEYTAR 

       490        500        510 
VHGWLDSTIK SGLTAARDVN RASQKPSRRQ LSNDNEL

« Hide

References

[1]"Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species."
St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.
Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ088990 mRNA. Translation: AAY89680.1.

3D structure databases

HSSPHSSP built from PDB template 2BXR based on UniProtKB P21397.
ProteinModelPortalQ4JHE3.
SMRQ4JHE3. Positions 23-505.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameOXLA_OXYSC
AccessionPrimary (citable) accession number: Q4JHE3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: August 2, 2005
Last modified: October 3, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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